Role of mTOR signalling in the control of translation initiation and elongation by nutrients.

作者: C. G. Proud

DOI: 10.1007/978-3-642-18930-2_13

关键词:

摘要: Protein synthesis requires nutrients both as precursors (amino acids) and a source of energy, since this process consumes high proportion cellular metabolic energy. Recent work has shown that types directly influence the activities components translational machinery in mammalian cells. Amino acids positively regulate signalling through target rapamycin (mTOR) pathway, although degree dependency on external amino varies between cell types. mTOR modulates several key involved mRNA translation, particular (via repressor proteins) cap-binding initiation factor eIF4E, ribosomal protein S6 kinases, elongation eEF2. The branched-chain acid leucine is most effective one It currently unclear how cells sense prevailing levels, may involve intracellular acids. Cellular ATP levels can also activity. some translation factors are modulated by mTOR-independent mechanisms. Examples include regulation eEF2 energy which be controlled via AMP-activated kinase, activity guanine nucleotide- exchange eIF2B, fuels.

参考文章(102)
Allen D. Everett, Tamara D. Stoops, Angus C. Nairn, David Brautigan, Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. American Journal of Physiology-heart and Circulatory Physiology. ,vol. 281, ,(2001) , 10.1152/AJPHEART.2001.281.1.H161
Malathy Mahalingam, Jonathan A. Cooper, Phosphorylation of Mammalian eIF4E by Mnk1 and Mnk2: Tantalizing Prospects for a Role in Translation Signaling Pathways for Translation. ,vol. 27, pp. 131- 142 ,(2001) , 10.1007/978-3-662-09889-9_5
N. T. Redpath, E. J. Foulstone, C. G. Proud, Regulation of translation elongation factor‐2 by insulin via a rapamycin‐sensitive signalling pathway. The EMBO Journal. ,vol. 15, pp. 2291- 2297 ,(1996) , 10.1002/J.1460-2075.1996.TB00582.X
Anne-Claude Gingras, Brian Raught, Nahum Sonenberg, Control of Translation by the Target of Rapamycin Proteins Signaling Pathways for Translation. ,vol. 27, pp. 143- 174 ,(2001) , 10.1007/978-3-662-09889-9_6
H.B. Jefferies, G. Thomas, G. Thomas, Elongation factor-1 alpha mRNA is selectively translated following mitogenic stimulation. Journal of Biological Chemistry. ,vol. 269, pp. 4367- 4372 ,(1994) , 10.1016/S0021-9258(17)41789-3
John WB Hershey, Michael Mathews, Nahum Sonenberg, None, Translational control of gene expression Cold Spring Harbor Laboratory Press. ,(2000)
Da-Qing Yang, Michael B. Kastan, Participation of ATM in insulin signalling through phosphorylation of eIF-4E-binding protein 1. Nature Cell Biology. ,vol. 2, pp. 893- 898 ,(2000) , 10.1038/35046542
Alex Toker, Alexandra C Newton, Cellular Signaling: Pivoting around PDK-1 Cell. ,vol. 103, pp. 185- 188 ,(2000) , 10.1016/S0092-8674(00)00110-0
D J Price, R A Nemenoff, J Avruch, Purification of a hepatic S6 kinase from cycloheximide-treated Rats. Journal of Biological Chemistry. ,vol. 264, pp. 13825- 13833 ,(1989) , 10.1016/S0021-9258(18)80075-8
G Miotto, R Venerando, K.K. Khurana, N Siliprandi, G.E. Mortimore, Control of hepatic proteolysis by leucine and isovaleryl-L-carnitine through a common locus. Evidence for a possible mechanism of recognition at the plasma membrane Journal of Biological Chemistry. ,vol. 267, pp. 22066- 22072 ,(1992) , 10.1016/S0021-9258(18)41636-5